Human Class I MHC HLA-A2 in complex with sorting nexin 24 (127-135) peptide KLSHQPVLL. Determined by X-ray diffraction at 2.08 Å resolution. Released 10 Jan 2024.
Explore 8TBW in 3D Show helices and sheets RCSB PDB PDBe
8TBW contains 25 α-helices and 60 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-12 | 10 | 1 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-54 | 5 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 133-135 | 3 | 1 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-174 | 11 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 3 |
| β-strand | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-224 | 3 | 4 |
| β-strand | 228-230 | 3 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-250 | 10 | 3 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-273 | 4 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 5 |
| α-helix | 5-6 | 2 | |
| β-strand | 7-12 | 6 | 6 |
| β-strand | 22-31 | 10 | 6 |
| β-strand | 32 | 1 | 5 |
| β-strand | 37-42 | 6 | 7 |
| β-strand | 45-46 | 2 | 7 |
| β-strand | 51-52 | 2 | 6 |
| α-helix | 53-55 | 3 | |
| β-strand | 56-57 | 2 | 6 |
| β-strand | 63-71 | 9 | 6 |
| β-strand | 79-84 | 6 | 7 |
| β-strand | 92-95 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-12 | 10 | 8 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 8 |
| β-strand | 31-37 | 7 | 8 |
| β-strand | 46-47 | 2 | 8 |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 8 |
| β-strand | 109-118 | 10 | 8 |
| β-strand | 121-126 | 6 | 8 |
| β-strand | 133-135 | 3 | 8 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-159 | 8 | |
| α-helix | 160-164 | 5 | |
| α-helix | 165-174 | 10 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 9 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-194 | 9 | 10 |
| β-strand | 198-208 | 11 | 10 |
| β-strand | 209 | 1 | 9 |
| β-strand | 214-219 | 6 | 11 |
| β-strand | 222-224 | 3 | 11 |
| β-strand | 228-230 | 3 | 10 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 10 |
| β-strand | 241-250 | 10 | 10 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 11 |
| β-strand | 270-273 | 4 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HLA-A*02:01 alpha chain | A, D | protein | 275 | Homo sapiens | A0A140T913 (AlphaFold model) |
| Beta-2-microglobulin | B, E | protein | 100 | Homo sapiens | P61769 (AlphaFold model) |
| Sorting nexin 24 (127-135) peptide | C, F | protein | 9 | Homo sapiens | Q9Y343 (AlphaFold model) |
>8TBW_1 HLA-A*02:01 alpha chain (chains A, D) GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYW DGETRKVKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETLQ RTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWE
>8TBW_2 Beta-2-microglobulin (chains B, E) MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>8TBW_3 Sorting nexin 24 (127-135) peptide (chains C, F) KLSHQPVLL
Accurate modeling of peptide-MHC structures with AlphaFold. Mikhaylov, V., Brambley, C.A., Keller, G.L.J. et al. Structure (2024) 32:228. DOI 10.1016/j.str.2023.11.011 · PubMed
Other PDB entries of the same protein (UniProt A0A140T913 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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